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Literature summary for 3.4.21.73 extracted from

  • Fleetwood, A.J.; Achuthan, A.; Schultz, H.; Nansen, A.; Almholt, K.; Usher, P.; Hamilton, J.A.
    Urokinase plasminogen activator is a central regulator of macrophage three-dimensional invasion, matrix degradation, and adhesion (2014), J. Immunol., 192, 3540-3547.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Mus musculus
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Mus musculus C57BL/6
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Synonyms

Synonyms Comment Organism
uPA
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Mus musculus
Urokinase plasminogen activator
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Mus musculus

General Information

General Information Comment Organism
malfunction macrophage adhesion to vitronectin is blocked by plasminogen activator inhibitor-1, which is also able to enhance in turn the two-dimensional migration on this matrix protein Mus musculus
physiological function urokinase plasminogen activator and its receptor coordinate a plasmin-mediated proteolytic cascade that is implicated in cell adhesion, cell motility, and matrix breakdown, for example, during inflammation. The enzyme is a central regulator of macrophage three-dimensional invasion, matrix degradation, and adhesion. Macrophage adhesion to vitronectin is enhanced by the enzyme. The enzyme's proteolytic activity is required for optimal macrophage three-dimensional invasion through a matrix barrier Mus musculus